KEGG   ENZYME: 3.2.1.152
Entry
EC 3.2.1.152                Enzyme                                 
Name
mannosylglycoprotein endo-beta-mannosidase;
endo-beta-mannosidase
Class
Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
Reaction(IUBMB)
Hydrolysis of the alpha-D-mannosyl-(1->6)-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl sequence of glycoprotein to alpha-D-mannosyl-(1->6)-D-mannose and N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl sequences
Comment
The substrate group is a substituent on N-4 of an asparagine residue in the glycoprotein. The mannose residue at the non-reducing end of the sequence may carry further alpha-D-mannosyl groups on O-3 or O-6, but such a substituent on O-3 of the beta-D-mannosyl group prevents the action of the enzyme. The enzyme was obtained from the lily, Lilium longiflorum.
History
EC 3.2.1.152 created 2005
Orthology
K18577  mannosylglycoprotein endo-beta-mannosidase
Genes
ATHAT1G09010
ALY9325794
CRB17900667
CSAT104739491 104755088 104767262
EUSEUTSA_v10006730mg
BRP103836364 103871635
BNA106346294 106362335 106415431 106453177
BOE106294903 106307139
RSZ108807750 108822974 130507228
THJ104805875
CPAP110815331
CIT102618119
CICCICLE_v10000150mg
PVY116118844 116128562
MINC123209656
TCC18600378
GRA105761023 105781536
GHI107887393 107893587 107920199 107958667
GAB108464371 108473723
HSYR120124249 120154013
DZI111277297 111295937
EGR104415555
GMX100787941 100804477 100809140 100817144
GSJ114370283 114400734 114402823 114407611
PVUPHAVU_006G092100g PHAVU_007G180100g
VRA106772076 106776242
VAR108342919 108345492
VUN114188276 114191121
VUM124836018 124837497
CCAJ109795453 109796169
APRC113861935 113872132
MTR11410041 11430551
TPRA123890901 123907349
CAM101503609 101505520
PSAT127098294 127132353
VVO131610606 131633928 131644094
LJALj1g3v4931610.1(Lj1g3v4931610.1) Lj5g3v1494660.1(Lj5g3v1494660.1)
ADU107465393 107492112
AIP107618043 107646499
AHF112710838 112758141 112775615
LANG109330117 109336087
PCIN129295024 129295874
QSAO6P43_007519
FVE101296018
RCN112192351
PPER18775253 18775314
PMUM103344631 103344633
PAVI110759657
PDUL117632383 117632384
MDM103450943 103451325
MSYL126592900 126592901
PXB103942899
ZJU107412022
CSAV115718737
CSV101207955
CMO103492174
BHJ120069814
MCHA111015278
CMAX111468316
CMOS111433409
CPEP111792852
RCU8285565
JCU105647543
HBR110644505
MESC110620745
POP7481756
PEU105125043
PALZ118060785
JRE109008073
CILL122317306
CAVE132168921
QSU111983211 111997616 112037497
QLO115979009
TWL120008957 120008958
VVI100254646
VRI117930200
SLY101267848
SPEN107008011
SOT102586571
SSTN125863851
SDUL129886193
CANN107854888
LBB132645908
NTA107762938 107828361
NSY104218593
NTO104105594
NAU109209905
INI109181437
ITR116005572
SIND105169398 105172345
OEU111389164 111411182
EGT105960789 105976210 105976346
SSPL121795360 121798907
SMIL130996919
APAN127260842
HAN110920122
ECAD122590961
LSV111895788
CCAV112507203
DCR108204287 108227635
CSIN114310720
RVL131334524 131334525
AEW130783446
BVG104890840
SOE110798590
CQI110708616
ATRI130797300
MOF131152684
NNU104596494
MING122057744
TSS122642219
PSOM113315242
OSA4338683
DOSAOs05t0391500-01(Os05g0391500)
OBR102703868
OGL127773687
BDI100834607
ATS109774075
TDC119277985 119341843
TAES123054439 123131312 123181888
TUA125516433
LPER127315760
LRD124647930 124707799
SBI8085086
ZMA103630319
SITA101785350
SVS117850534
PVIR120665611 120698819
PHAI112885781
PDA103716435
EGU105057570
MUS103977642
ZOF121988714 121997643
DCT110098097 110114017
PEQ110021821 110023222
AOF109840056
MSIN131226012
NCOL116258708
ATR18440882
SMOSELMODRAFT_155695 SELMODRAFT_164536
PPP112285782 112292500
CSLCOCSUDRAFT_28678
TPSTHAPSDRAFT_262343
EHXEMIHUDRAFT_231619
GTTGUITHDRAFT_64741
BURBcep18194_C7540
BCONNL30_34310
BMECWJ16_19375
PMEGFNZ07_11640
BCELBcellWH2_02649(csxA_3)
PMUCING2E5A_0455(EBM)
PSACPSM36_0848 PSM36_1079
PDIBDI_3381
PARCCI960_23000
AITAI2BBH_10670
MCOSGM418_24495
CPICpin_2275
CHIHGWR21_26635
CFILMYF79_27920
NKONiako_7278
NSONIASO_18765
NIAA8C56_16950
FLASY85_05335
AGIFSB73_19460
ARACE0W69_005870
FLNFLA_4835
PSEGD3H65_04885
PCMAY601_2523
PEKFFJ24_022710
PROEH9L23_23000
SHGSph21_1452
MUPA0256_20255
MUCMuYL_1839
MGOTMgSA37_01958(csxA_3)
MUHHYN43_006850
MGINFRZ54_16465
MGKFSB76_29410
MRUBDEO27_007190
MGOSDIU38_007020
MMABHQ865_04360
OLIFKG96_04205
SBXCA265_21990
EVIEchvi_3868
ESTDN752_02690
SPIKEXU85_03505
SRHOHH216_15960
HYZAXW84_06640
HNVDDQ68_00540
RUDTH61_17245
NIBGU926_04950
ZPRZPR_4166
SPONHME9304_00657(csxA)
 » show all
Reference
1  [PMID:15247239]
  Authors
Ishimizu T, Sasaki A, Okutani S, Maeda M, Yamagishi M, Hase S
  Title
Endo-beta-mannosidase, a plant enzyme acting on N-glycan: purification, molecular cloning, and characterization.
  Journal
J Biol Chem 279:38555-62 (2004)
DOI:10.1074/jbc.M406886200
  Sequence
[ath:AT1G09010]
Reference
2  [PMID:9990135]
  Authors
Sasaki A, Yamagishi M, Mega T, Norioka S, Natsuka S, Hase S.
  Title
Partial purification and characterization of a novel endo-beta-mannosidase acting on N-linked sugar chains from Lilium longflorum thumb.
  Journal
J Biochem (Tokyo) 125:363-7 (1999)
DOI:10.1093/oxfordjournals.jbchem.a022295
Other DBs
ExplorEnz - The Enzyme Database: 3.2.1.152
IUBMB Enzyme Nomenclature: 3.2.1.152
ExPASy - ENZYME nomenclature database: 3.2.1.152
BRENDA, the Enzyme Database: 3.2.1.152
CAS: 141176-95-6

DBGET integrated database retrieval system